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• W1698064934 abstract "Abstract Background SCF ubiquitin ligases target numerous proteins for ubiquitin dependent proteolysis, including p27 and cyclin E. SCF and other cullin-RING ligases (CRLs) are regulated by the ubiquitin-like protein Nedd8 that covalently modifies the cullin subunit. The removal of Nedd8 is catalyzed by the Jab1/MPN domain metalloenzyme (JAMM) motif within the Csn5 subunit of the Cop9 Signalosome. Results Here, we conditionally knock down Csn5 expression in HEK293 human cells using a doxycycline-inducible shRNA system. Cullin levels were not altered in CSN-deficient human cells, but the levels of multiple F-box proteins were decreased. Molecular analysis indicates that this decrease was due to increased Cul1- and proteasome-dependent turnover. Diminished F-box levels resulted in reduced SCF activity, as evidenced by accumulation of two substrates of the F-box protein Fbw7, cyclin E and c-myc, in Csn5-depleted cells. Conclusion We propose that deneddylation of Cul1 is required to sustain optimal activity of SCF ubiquitin ligases by repressing 'autoubiquitination' of F-box proteins within SCF complexes, thereby rescuing them from premature degradation." @default.
• W1698064934 created "2016-06-24" @default.
• W1698064934 creator A5008197255 @default.
• W1698064934 creator A5066867755 @default.
• W1698064934 date "2006-01-09" @default.
• W1698064934 modified "2023-09-27" @default.
• W1698064934 title "Targeted silencing of Jab1/Csn5 in human cells downregulates SCF activity through reduction of F-box protein levels" @default.
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• W1698064934 doi "https://doi.org/10.1186/1471-2091-7-1" @default.
• W1698064934 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/1360668" @default.
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